THIX_ALKHC
ID THIX_ALKHC Reviewed; 250 AA.
AC Q9K9G6;
DT 07-JAN-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 106.
DE RecName: Full=Formylaminopyrimidine transport permease protein ThiX {ECO:0000305};
DE Short=FAMP transport permease protein {ECO:0000305};
GN Name=thiX {ECO:0000303|PubMed:17618314};
GN OrderedLocusNames=BH2681 {ECO:0000312|EMBL:BAB06400.1};
OS Alkalihalobacillus halodurans (strain ATCC BAA-125 / DSM 18197 / FERM 7344
OS / JCM 9153 / C-125) (Bacillus halodurans).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Alkalihalobacillus.
OX NCBI_TaxID=272558;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM 9153 / C-125;
RX PubMed=11058132; DOI=10.1093/nar/28.21.4317;
RA Takami H., Nakasone K., Takaki Y., Maeno G., Sasaki R., Masui N., Fuji F.,
RA Hirama C., Nakamura Y., Ogasawara N., Kuhara S., Horikoshi K.;
RT "Complete genome sequence of the alkaliphilic bacterium Bacillus halodurans
RT and genomic sequence comparison with Bacillus subtilis.";
RL Nucleic Acids Res. 28:4317-4331(2000).
RN [2]
RP FUNCTION, AND PATHWAY.
RX PubMed=17618314; DOI=10.1038/nchembio.2007.13;
RA Jenkins A.H., Schyns G., Potot S., Sun G., Begley T.P.;
RT "A new thiamin salvage pathway.";
RL Nat. Chem. Biol. 3:492-497(2007).
CC -!- FUNCTION: Participates in a thiamine pyrimidine salvage pathway as part
CC of the ABC transporter complex ThiXYZ involved in the import of
CC thiamine degradation products such as the formylaminopyrimidine N-
CC formyl-4-amino-5-aminomethyl-2-methylpyrimidine (FAMP). Is probably
CC responsible for the translocation of the substrate across the membrane.
CC {ECO:0000303|PubMed:17618314, ECO:0000305}.
CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis.
CC {ECO:0000303|PubMed:17618314}.
CC -!- SUBUNIT: The complex is likely composed of an ATP-binding protein
CC (ThiZ), a transmembrane protein (ThiX) and a solute-binding protein
CC (ThiY). {ECO:0000303|PubMed:17618314, ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255}; Multi-pass membrane
CC protein {ECO:0000255}.
CC -!- SIMILARITY: Belongs to the binding-protein-dependent transport system
CC permease family. {ECO:0000305}.
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DR EMBL; BA000004; BAB06400.1; -; Genomic_DNA.
DR PIR; A83985; A83985.
DR RefSeq; WP_010898830.1; NC_002570.2.
DR AlphaFoldDB; Q9K9G6; -.
DR SMR; Q9K9G6; -.
DR STRING; 272558.10175302; -.
DR EnsemblBacteria; BAB06400; BAB06400; BAB06400.
DR KEGG; bha:BH2681; -.
DR eggNOG; COG0600; Bacteria.
DR HOGENOM; CLU_046113_2_1_9; -.
DR OMA; LDIPRMF; -.
DR OrthoDB; 916788at2; -.
DR UniPathway; UPA00060; -.
DR Proteomes; UP000001258; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0055085; P:transmembrane transport; IEA:InterPro.
DR CDD; cd06261; TM_PBP2; 1.
DR Gene3D; 1.10.3720.10; -; 1.
DR InterPro; IPR000515; MetI-like.
DR InterPro; IPR035906; MetI-like_sf.
DR Pfam; PF00528; BPD_transp_1; 1.
DR SUPFAM; SSF161098; SSF161098; 1.
DR PROSITE; PS50928; ABC_TM1; 1.
PE 3: Inferred from homology;
KW Cell membrane; Membrane; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..250
FT /note="Formylaminopyrimidine transport permease protein
FT ThiX"
FT /id="PRO_0000431516"
FT TRANSMEM 5..25
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TRANSMEM 62..82
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TRANSMEM 94..114
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TRANSMEM 115..135
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TRANSMEM 172..192
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TRANSMEM 216..236
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT DOMAIN 56..237
FT /note="ABC transmembrane type-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
SQ SEQUENCE 250 AA; 28147 MW; 1D32097DB7BCBFD8 CRC64;
MKRSYQALEP TLFFLMLMVI WEISARMIGQ PYLLPSPIQI VMRTIDLSES LFFTHLPATL
AIISIGLALS IVLGILLSLL MFWNERVERA VYPLLVASQT IPVIALAPIF VLWFGYSIWS
KVAVTVLLTF FPITVNTYDG LKSTNRQYEE LFYTMGATKR QLFYRLFVPS TLPSFLTGLR
IAVPLAVIGA AVGEWLGANE GLGYFSRRMM TQFDGPGVFA PIFILSLLGI LGFAAIKKLE
NILLPWRKKQ
